| + |
PRKACA | down-regulates activity 
phosphorylation
|
STK38 |
0.299 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-276391 |
Ser10 |
MTGSTPCsSMSNHTK |
in vitro |
|
| pmid |
sentence |
| 22142472 |
GSK-3β phosphorylated STK38 on residues S6 and T7 in vitro, depending largely on a PKA-mediated priming phosphorylation of STK38 on residues S10 and S11, respectively. Our results indicate that that GSK-3β inhibits STK38's full activation, and suggest that STK38 activation is required to prevent cell death in response to oxidative stress. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-276390 |
Ser11 |
TGSTPCSsMSNHTKE |
in vitro |
|
| pmid |
sentence |
| 22142472 |
GSK-3β phosphorylated STK38 on residues S6 and T7 in vitro, depending largely on a PKA-mediated priming phosphorylation of STK38 on residues S10 and S11, respectively. Our results indicate that that GSK-3β inhibits STK38's full activation, and suggest that STK38 activation is required to prevent cell death in response to oxidative stress. |
|
| Publications: |
2 |
Organism: |
In Vitro |
| + |
STK38 | up-regulates activity 
phosphorylation
|
XPO1 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-277483 |
Ser1055 |
EKHKRQMsVPGIFNP |
Homo sapiens |
HeLa Cell |
| pmid |
sentence |
| 31544310 |
We further uncover that STK38 modulates XPO1 export activity by phosphorylating XPO1 on serine 1055, thus regulating its own nuclear exit. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
STK38 | down-regulates activity
phosphorylation
|
YAP1 |
0.393 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-259856 |
Ser109 |
KSHSRQAsTDAGTAG |
Homo sapiens |
|
| pmid |
sentence |
| 25601544 |
We performed mass spectrometry to determine additional sites on YAP1 targeted by NDR, identifying three additional serines, namely S61, S109, and S164, to also be phosphorylated by NDR in vitro |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-259855 |
Ser127 |
PQHVRAHsSPASLQL |
Homo sapiens |
|
| pmid |
sentence |
| 25601544 |
We show that mammalian NDR1/2 kinases phosphorylate YAP1 on S127 and thereby negatively regulate YAP1 activity in tissue-cultured cells. |
|
| Publications: |
2 |
Organism: |
Homo Sapiens |
| + |
STK38 | down-regulates quantity by destabilization
phosphorylation
|
CDKN1A |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-272961 |
Ser146 |
GRKRRQTsMTDFYHS |
Homo sapiens |
HEK-293 Cell |
| pmid |
sentence |
| 21262772 |
More importantly, with the direct regulation of p21 stability by phosphorylation on Ser 146, we define here the first downstream signaling mechanisms by which NDR kinases can control G1/S progression.|NDR kinases regulate p21 stability by phosphorylation of S146 on p21. | |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
STK38 | up-regulates activity
phosphorylation
|
PI4KB |
0.27 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-263033 |
Ser277 |
RTHQRSKsDATASIS |
Mus musculus |
|
| pmid |
sentence |
| 22445341 |
We identified 5 potential NDR1 substrates in the mouse brain and chose two for functional validation. We show that one NDR1 substrate is another kinase, AP-2 associated kinase-1 (AAK1) which regulates dendritic branching as a result of NDR1 phosphorylation. Another substrate is the Rab8 guanine nucleotide exchange factor (GEF) Rabin8 (a Sec2p homolog) which we find is involved in spine synapse formation. |
|
| Publications: |
1 |
Organism: |
Mus Musculus |
| Tissue: |
Brain |
| + |
STK38 | up-regulates
phosphorylation
|
STK38 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-96679 |
Ser281 |
NRRQLAFsTVGTPDY |
Homo sapiens |
|
| pmid |
sentence |
| 12493777 |
We found that ndr1 autophosphorylates in vitro predominantly on ser-281 and to a lesser extent on thr-74 and thr-444. All of these residues proved to be crucial also for ndr1 activity in vivo |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-142514 |
Ser281 |
NRRQLAFsTVGTPDY |
Homo sapiens |
HEK-293 Cell |
| pmid |
sentence |
| 16314523 |
Ndr1/ndr2 protein kinase is activated by phosphorylation on the activation loop phosphorylation site ser281/ser282 and the hydrophobic motif phosphorylation site thr444/thr442. Autophosphorylation of ndr is responsible for phosphorylation on ser281/ser282, whereas thr444/thr442 is targeted by an upstream kinase. Here we show that mst3, a mammalian ste20-like protein kinase, is able to phosphorylate ndr protein kinase at thr444/thr442. In vitro, mst3 selectively phosphorylated thr442 of ndr2, resulting in a 10-fold stimulation of ndr activity. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-96683 |
Thr444 |
DWVFINYtYKRFEGL |
Homo sapiens |
|
| pmid |
sentence |
| 12493777 |
We found that ndr1 autophosphorylates in vitro predominantly on ser-281 and to a lesser extent on thr-74 and thr-444. All of these residues proved to be crucial also for ndr1 activity in vivo |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-96687 |
Thr74 |
SAHARKEtEFLRLKR |
Homo sapiens |
|
| pmid |
sentence |
| 12493777 |
We found that ndr1 autophosphorylates in vitro predominantly on ser-281 and to a lesser extent on thr-74 and thr-444. All of these residues proved to be crucial also for ndr1 activity in vivo |
|
| Publications: |
4 |
Organism: |
Homo Sapiens |
| + |
STK38 | up-regulates activity
phosphorylation
|
RAB3IP |
0.375 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-263036 |
Ser288 |
KGHTRNKsTSSAMSG |
Mus musculus |
|
| pmid |
sentence |
| 22445341 |
We identified 5 potential NDR1 substrates in the mouse brain and chose two for functional validation. We show that one NDR1 substrate is another kinase, AP-2 associated kinase-1 (AAK1) which regulates dendritic branching as a result of NDR1 phosphorylation. Another substrate is the Rab8 guanine nucleotide exchange factor (GEF) Rabin8 (a Sec2p homolog) which we find is involved in spine synapse formation. |
|
| Publications: |
1 |
Organism: |
Mus Musculus |
| Tissue: |
Brain |
| + |
STK38 | up-regulates activity
phosphorylation
|
RAB11FIP5 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-263035 |
Ser307 |
FTHKRTYsDEANQMR |
Mus musculus |
|
| pmid |
sentence |
| 22445341 |
We identified 5 potential NDR1 substrates in the mouse brain and chose two for functional validation. We show that one NDR1 substrate is another kinase, AP-2 associated kinase-1 (AAK1) which regulates dendritic branching as a result of NDR1 phosphorylation. Another substrate is the Rab8 guanine nucleotide exchange factor (GEF) Rabin8 (a Sec2p homolog) which we find is involved in spine synapse formation. |
|
| Publications: |
1 |
Organism: |
Mus Musculus |
| Tissue: |
Brain |
| + |
STK38 | up-regulates activity
phosphorylation
|
PANX2 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-263032 |
Ser514 |
KKHARHFsLDVHPYI |
Mus musculus |
|
| pmid |
sentence |
| 22445341 |
We identified 5 potential NDR1 substrates in the mouse brain and chose two for functional validation. We show that one NDR1 substrate is another kinase, AP-2 associated kinase-1 (AAK1) which regulates dendritic branching as a result of NDR1 phosphorylation. Another substrate is the Rab8 guanine nucleotide exchange factor (GEF) Rabin8 (a Sec2p homolog) which we find is involved in spine synapse formation. |
|
| Publications: |
1 |
Organism: |
Mus Musculus |
| Tissue: |
Brain |
| + |
GSK3B | down-regulates activity
phosphorylation
|
STK38 |
0.281 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-276392 |
Ser6 |
sTPCSSMS |
in vitro |
|
| pmid |
sentence |
| 22142472 |
GSK-3β phosphorylated STK38 on residues S6 and T7 in vitro, depending largely on a PKA-mediated priming phosphorylation of STK38 on residues S10 and S11, respectively. Our results indicate that that GSK-3β inhibits STK38's full activation, and suggest that STK38 activation is required to prevent cell death in response to oxidative stress. |
|
| Publications: |
1 |
Organism: |
In Vitro |
| + |
STK38 | up-regulates activity
phosphorylation
|
AAK1 |
0.274 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-263034 |
Ser637 |
AGHRRILsDVTHSAV |
Mus musculus |
|
| pmid |
sentence |
| 22445341 |
We identified 5 potential NDR1 substrates in the mouse brain and chose two for functional validation. We show that one NDR1 substrate is another kinase, AP-2 associated kinase-1 (AAK1) which regulates dendritic branching as a result of NDR1 phosphorylation. Another substrate is the Rab8 guanine nucleotide exchange factor (GEF) Rabin8 (a Sec2p homolog) which we find is involved in spine synapse formation. AAK1 phosphorylation regulates dendrite branching and length |
|
| Publications: |
1 |
Organism: |
Mus Musculus |
| Tissue: |
Brain |
| + |
PLK1 | down-regulates activity
phosphorylation
|
STK38 |
0.321 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-276913 |
Thr183 |
TLLMKKDtLTEEETQ |
Homo sapiens |
HeLa Cell |
| pmid |
sentence |
| 26057687 |
Here, we identified a conserved signaling axis in which NDR1 kinase activity is regulated by PLK1 in mitosis. PLK1 phosphorylates NDR1 at three putative threonine residues (T7, T183 and T407) at mitotic entry, which elicits PLK1-dependent suppression of NDR1 activity and ensures correct spindle orientation in mitosis. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-276915 |
Thr407 |
EIKSIDDtSNFDEFP |
Homo sapiens |
HeLa Cell |
| pmid |
sentence |
| 26057687 |
Here, we identified a conserved signaling axis in which NDR1 kinase activity is regulated by PLK1 in mitosis. PLK1 phosphorylates NDR1 at three putative threonine residues (T7, T183 and T407) at mitotic entry, which elicits PLK1-dependent suppression of NDR1 activity and ensures correct spindle orientation in mitosis. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-276914 |
Thr7 |
tPCSSMSN |
Homo sapiens |
HeLa Cell |
| pmid |
sentence |
| 26057687 |
Here, we identified a conserved signaling axis in which NDR1 kinase activity is regulated by PLK1 in mitosis. PLK1 phosphorylates NDR1 at three putative threonine residues (T7, T183 and T407) at mitotic entry, which elicits PLK1-dependent suppression of NDR1 activity and ensures correct spindle orientation in mitosis. |
|
| Publications: |
3 |
Organism: |
Homo Sapiens |
| + |
STK24 | up-regulates
phosphorylation
|
STK38 |
0.39 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-142467 |
Thr444 |
DWVFINYtYKRFEGL |
Homo sapiens |
HEK-293 Cell |
| pmid |
sentence |
| 16314523 |
Ndr1/ndr2 protein kinase is activated by phosphorylation on the activation loop phosphorylation site ser281/ser282 and the hydrophobic motif phosphorylation site thr444/thr442. Autophosphorylation of ndr is responsible for phosphorylation on ser281/ser282, whereas thr444/thr442 is targeted by an upstream kinase. Here we show that mst3, a mammalian ste20-like protein kinase, is able to phosphorylate ndr protein kinase at thr444/thr442. In vitro, mst3 selectively phosphorylated thr442 of ndr2, resulting in a 10-fold stimulation of ndr activity. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
3.0
STK38
- 
- 